Expression of heat shock proteins in osteosarcoma and its relationship to prognosis
- PMID: 11087053
- DOI: 10.1016/S0344-0338(00)80118-1
Expression of heat shock proteins in osteosarcoma and its relationship to prognosis
Abstract
The prognosis of osteosarcoma has been improved by chemotherapy. Heat shock proteins (HSPs) assist in folding proteins at posttranslation and degeneration under stress. We investigated the effect of HSPs on survival in osteosarcoma. Conventional osteosarcomas of the extremities from 70 patients aged 30 years or younger were used. Preoperational chemotherapy was performed in all cases. Tissues at surgery and biopsy were immunohistochemically stained with anti-HSP27, HSP47, HSP60, HSP70, HSP90alpha, HSP90beta, and p53 antibodies. We classified the cases in which more than 10% of tumor cells were positive into the overexpressing group. Overall survival was compared between the groups either overexpressing HSPs or not using Wilcoxon's test and Cox's proportional hazard model. The overexpression rate at biopsy was 22% (HSP27), 88% (HSP47), 66% (HSP60), 48% (HSP70(, 47% (HSP90alpha), 31% (HSP90beta), and 17% (p53), respectively. The rate at surgery was 33% (HSP27), 94% (HSP47), 60% (HSP60), 49% (HSP70), 28% (HSP90alpha), 40% (HSP90beta), and 17% (p53), respectively. HSP27 and p53 overexpression at biopsy had a negative prognostic value. HSP27 showed the strongest negative prognostic value in osteosarcoma. It is therefore important to investigate further its function in cellular regulation and drug resistance.
Similar articles
-
Expression of heat shock proteins in osteosarcomas.Pathology. 2010;42(5):421-5. doi: 10.3109/00313025.2010.493866. Pathology. 2010. PMID: 20632817
-
Overexpression of resistance-related proteins (metallothioneins, glutathione-S-transferase pi, heat shock protein 27, and lung resistance-related protein) in osteosarcoma. Relationship with poor prognosis.Cancer. 1997 Jun 15;79(12):2336-44. doi: 10.1002/(sici)1097-0142(19970615)79:12<2336::aid-cncr7>3.0.co;2-j. Cancer. 1997. PMID: 9191521
-
Heat shock protein expression independently predicts clinical outcome in prostate cancer.Cancer Res. 2000 Dec 15;60(24):7099-105. Cancer Res. 2000. PMID: 11156417
-
Molecular Chaperones in Osteosarcoma: Diagnosis and Therapeutic Issues.Cells. 2021 Mar 30;10(4):754. doi: 10.3390/cells10040754. Cells. 2021. PMID: 33808130 Free PMC article. Review.
-
The role of heat shock proteins in cancer.Cancer Lett. 2015 May 1;360(2):114-8. doi: 10.1016/j.canlet.2015.02.026. Epub 2015 Feb 23. Cancer Lett. 2015. PMID: 25721081 Review.
Cited by
-
Phosphorylated heat shock protein 27 as a potential biomarker to predict the role of chemotherapy-induced autophagy in osteosarcoma response to therapy.Oncotarget. 2017 Aug 17;9(2):1602-1616. doi: 10.18632/oncotarget.20308. eCollection 2018 Jan 5. Oncotarget. 2017. PMID: 29416717 Free PMC article.
-
Identification of proteomic differences between squamous cell carcinoma of the lung and bronchial epithelium.Mol Cell Proteomics. 2009 May;8(5):1105-16. doi: 10.1074/mcp.M800422-MCP200. Epub 2009 Jan 27. Mol Cell Proteomics. 2009. PMID: 19176476 Free PMC article.
-
Revisiting the seed and soil in cancer metastasis.Int J Biochem Cell Biol. 2009 Jul;41(7):1452-62. doi: 10.1016/j.biocel.2009.01.015. Epub 2009 Feb 3. Int J Biochem Cell Biol. 2009. PMID: 19401145 Free PMC article. Review.
-
Targeting protein quality control pathways in breast cancer.BMC Biol. 2017 Nov 16;15(1):109. doi: 10.1186/s12915-017-0449-4. BMC Biol. 2017. PMID: 29145850 Free PMC article. Review.
-
HSPD1 Supports Osteosarcoma Progression through Stabilizing ATP5A1 and thus Activation of AKT/mTOR Signaling.Int J Biol Sci. 2024 Sep 23;20(13):5162-5190. doi: 10.7150/ijbs.100015. eCollection 2024. Int J Biol Sci. 2024. PMID: 39430254 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Medical
Research Materials
Miscellaneous
